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TitleMultiple independent acquisitions of ACE2 usage in MERS-related coronaviruses.
Journal, issue, pagesCell, Vol. 188, Issue 6, Page 1693-1710.e18, Year 2025
Publish dateMar 20, 2025
AuthorsCheng-Bao Ma / Chen Liu / Young-Jun Park / Jingjing Tang / Jing Chen / Qing Xiong / Jimin Lee / Cameron Stewart / Daniel Asarnow / Jack Brown / M Alejandra Tortorici / Xiao Yang / Ye-Hui Sun / Yuan-Mei Chen / Xiao Yu / Jun-Yu Si / Peng Liu / Fei Tong / Mei-Ling Huang / Jing Li / Zheng-Li Shi / Zengqin Deng / David Veesler / Huan Yan /
PubMed AbstractThe angiotensin-converting enzyme 2 (ACE2) receptor is shared by various coronaviruses with distinct receptor-binding domain (RBD) architectures, yet our understanding of these convergent acquisition ...The angiotensin-converting enzyme 2 (ACE2) receptor is shared by various coronaviruses with distinct receptor-binding domain (RBD) architectures, yet our understanding of these convergent acquisition events remains elusive. Here, we report that two bat MERS-related coronaviruses (MERSr-CoVs) infecting Pipistrellus nathusii (P.nat)-MOW15-22 and PnNL2018B-use ACE2 as their receptor, with narrow ortholog specificity. Cryoelectron microscopy structures of the MOW15-22/PnNL2018B RBD-ACE2 complexes unveil an unexpected and entirely distinct binding mode, mapping >45 Å away from that of any other known ACE2-using coronaviruses. Functional profiling of ACE2 orthologs from 105 mammalian species led to the identification of host tropism determinants, including an ACE2 N432-glycosylation restricting viral recognition, and the design of a soluble P.nat ACE2 mutant with potent viral neutralizing activity. Our findings reveal convergent acquisition of ACE2 usage for merbecoviruses found in European bats, underscoring the extraordinary diversity of ACE2 recognition modes among coronaviruses and the promiscuity of this receptor.
External linksCell / PubMed:39922191
MethodsEM (single particle)
Resolution2.4 - 3.31 Å
Structure data

45253

9c6o

EMDB-45253, PDB-9c6o:
Merbecovirus MOW15-22 Spike glycoprotein RBD bound to the P. davyi ACE2
Method: EM (single particle) / Resolution: 2.77 Å

46691

9dak

EMDB-46691, PDB-9dak:
Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2
Method: EM (single particle) / Resolution: 2.4 Å

60483

8zuf

EMDB-60483, PDB-8zuf:
Cryo-EM structure of P.nat ACE2 mutant in complex with MOW15-22 RBD
Method: EM (single particle) / Resolution: 3.31 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • Sarbecovirus
  • merbecovirus
  • pteronotus davyi (Davy's naked-backed bat)
  • pipistrellus nathusii (Nathusius's pipistrelle)
  • middle east respiratory syndrome-related coronavirus
KeywordsVIRAL PROTEIN/HYDROLASE / ACE2 / RBD / VIRAL PROTEIN-HYDROLASE complex / VIRAL PROTEIN / Merbecovirus / MERS-related coronaviruses / MOW15-22 Spike glycoprotein / fusion protein / P. davyi ACE2 / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / Spike glycoprotein / inhibitor

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